Reviewed, UniProtKB/Swiss-Prot P01190 (COLI_BOVIN)

Names and origin

Protein names

Recommended name:
    Pro-opiomelanocortin
      Short name=POMC
Alternative name(s):
    Corticotropin-lipotropin
Cleaved into the following 10 chains:
    1- Recommended name:
            NPP
    2- Recommended name:
            Melanotropin gamma
        Alternative name(s):
            Gamma-MSH
    3- Recommended name:
            Corticotropin
        Alternative name(s):
            Adrenocorticotropic hormone
              Short name=ACTH
    4- Recommended name:
            Melanotropin alpha
        Alternative name(s):
            Alpha-MSH
    5- Recommended name:
            Corticotropin-like intermediary peptide
                Short name=CLIP
    6- Recommended name:
            Lipotropin beta
        Alternative name(s):
            Beta-LPH
    7- Recommended name:
            Lipotropin gamma
        Alternative name(s):
            Gamma-LPH
    8- Recommended name:
            Melanotropin beta
        Alternative name(s):
            Beta-MSH
    9- Recommended name:
            Beta-endorphin
    10- Recommended name:
            Met-enkephalin

Gene names

Name:

POMC

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	265 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	ACTH stimulates the adrenal glands to release cortisol. MSH (melanocyte-stimulating hormone) increases the pigmentation of skin by increasing melanin production in melanocytes. Beta-endorphin and Met-enkephalin are endogenous opiates.
Tissue specificity	ACTH and MSH are produced by the pituitary gland.
Post-translational modification	Specific enzymatic cleavages at paired basic residues yield the different active peptides.
Sequence similarities	Belongs to the POMC family.

Ontologies

Keywords
Domain	Signal
Molecular function	Endorphin Hormone
PTM	Amidation Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Pyrrolidone carboxylic acid Sulfation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	neuropeptide signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	hormone activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	By similarity
	Peptide	27 – 103	77	NPP		PRO_0000024943
	Peptide	77 – 87	11	Melanotropin gamma		PRO_0000024944
	Propeptide	106 – 129	24			PRO_0000024945
	Peptide	132 – 170	39	Corticotropin		PRO_0000024946
	Peptide	132 – 144	13	Melanotropin alpha		PRO_0000024947
	Peptide	150 – 170	21	Corticotropin-like intermediary peptide		PRO_0000024948
	Peptide	173 – 265	93	Lipotropin beta		PRO_0000024949
	Peptide	173 – 232	60	Lipotropin gamma		PRO_0000024950
	Peptide	215 – 232	18	Melanotropin beta		PRO_0000024951
	Peptide	235 – 265	31	Beta-endorphin		PRO_0000024952
	Peptide	235 – 239	5	Met-enkephalin		PRO_0000024953
Amino acid modifications
	Modified residue	87	1	Phenylalanine amide Ref.7
	Modified residue	144	1	Valine amide
	Modified residue	162	1	Phosphoserine By similarity
	Modified residue	173	1	Pyrrolidone carboxylic acid (Glu); partial
	Modified residue	200	1	Sulfotyrosine
	Glycosylation	71	1	O-linked (GalNAc...) Ref.15		CAR_000202
	Glycosylation	91	1	N-linked (GlcNAc...) Ref.15		CAR_000034
	Disulfide bond	28 ↔ 50		Ref.15
	Disulfide bond	34 ↔ 46		Ref.15
Experimental info
	Sequence conflict	10	1	G → A in AAA30354. Ref.2
	Sequence conflict	139	1	R → P in AAA30354. Ref.2
	Sequence conflict	161	1	Missing in AAA30718. Ref.6
	Sequence conflict	188	1	Q → G may be a typographical error Ref.11
	Sequence conflict	190 – 191	2	ES → D in AAA30718. Ref.6
	Sequence conflict	196	1	A → P in AAA30354. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P01190-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 303E9A0BCB073B3F	FASTA	265	29,260
	10 20 30 40 50 60 MPRLCSSRSG ALLLALLLQA SMEVRGWCLE SSQCQDLTTE SNLLACIRAC KPDLSAETPV 70 80 90 100 110 120 FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NGSSSSGVGG AAQKREEEVA VGEGPGPRGD 130 140 150 160 170 180 DAETGPREDK RSYSMEHFRW GKPVGKKRRP VKVYPNGAED ESAQAFPLEF KRELTGERLE 190 200 210 220 230 240 QARGPEAQAE SAAARAELEY GLVAEAEAEA AEKKDSGPYK MEHFRWGSPP KDKRYGGFMT 250 260 SEKSQTPLVT LFKNAIIKNA HKKGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of cloned cDNA for bovine corticotropin-beta-lipotropin precursor." Nakanishi S., Inoue A., Kita T., Nakamura M., Chang A.C.Y., Cohen S.N., Numa S. Nature 278:423-427(1979) [PubMed: 221818] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Studies of cloned DNA encoding the structure for the bovine corticotropin-beta-lipotropin precursor protein." Cohen S.N., Chang A.C.Y., Nakanishi S., Inoue A., Kita T., Nakamura M., Numa S. Ann. N. Y. Acad. Sci. 343:415-425(1980) [PubMed: 6249166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Isolation and characterization of the bovine corticotropin/beta-lipotropin precursor gene." Nakanishi S., Teranishi Y., Watanabe Y., Notake M., Noda M., Kakidani H., Jingami H., Numa S. Eur. J. Biochem. 115:429-438(1981) [PubMed: 6263630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Hypothalamus.
[5]	"Genetic engineering of peptide hormones." Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S., Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V., Zhvirblis G.S., Skryabin K.G., Baev A.A. Mol. Biol. (Mosk.) 19:226-235(1985) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-265.
[6]	"Construction of bacterial plasmids that contain the nucleotide sequence for bovine corticotropin-beta-lipotropin precursor." Nakanishi G., Inoue A., Kita T., Numa S., Chang A.C.Y., Cohen S.N., Nunberg J., Schimke R.T. Proc. Natl. Acad. Sci. U.S.A. 75:6021-6025(1978) [PubMed: 216007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 132-200.
[7]	"Isolation and characterization of a gamma 1-melanotropin-like peptide from bovine neurointermediate pituitary." Boehlen P., Esch F., Shibasaki T., Baird A., Ling N., Guillemin R. FEBS Lett. 128:67-70(1981) [PubMed: 7274457] [Abstract] Cited for: PROTEIN SEQUENCE OF 77-87.
[8]	"The relation of chemical structure to the biologic activity of pituitary hormones." Li C.H. Lab. Invest. 8:574-587(1959) [PubMed: 13642798] [Abstract] Cited for: PROTEIN SEQUENCE OF 131-144.
[9]	"Isolation of melatonin, the pineal gland factor that lightens melanocytes." Li C.H., Dixon J.S., Chung D. J. Am. Chem. Soc. 80:2587-2588(1958) Cited for: PROTEIN SEQUENCE OF 132-170.
[10]	"Adrenocorticotropin 45. Revised amino acid sequences for sheep and bovine hormones." Li C.H. Biochem. Biophys. Res. Commun. 49:835-839(1972) [PubMed: 4344689] [Abstract] Cited for: SEQUENCE REVISION (CORTICOTROPIN).
[11]	"Primary structure of the bovine beta-lipotropic hormone." Pankov Y.A. Vopr. Med. Khim. 19:330-332(1973) Cited for: PROTEIN SEQUENCE OF 173-265.
[12]	"The isolation and structure of a melanocyte-stimulating hormone from bovine pituitary glands." Geschwind I.I., Li C.H., Barnafi L. J. Am. Chem. Soc. 79:1003-1004(1957) Cited for: PROTEIN SEQUENCE OF 215-232.
[13]	"Amino-acid sequence of a melanophore-stimulating peptide." Harris J.I., Roos P. Nature 178:90-90(1956) [PubMed: 13348631] [Abstract] Cited for: PROTEIN SEQUENCE OF 215-232.
[14]	"Morphine-like peptides in mammalian brain: isolation, structure elucidation, and interactions with the opiate receptor." Simantov R., Snyder S.H. Proc. Natl. Acad. Sci. U.S.A. 73:2515-2519(1976) [PubMed: 1065904] [Abstract] Cited for: PROTEIN SEQUENCE OF 235-239.
[15]	"Use of reversed-phase and ion-exchange batch extraction in the purification of bovine pituitary peptides." James S., Bennett H.P.J. J. Chromatogr. A 326:329-338(1985) [PubMed: 4030947] [Abstract] Cited for: GLYCOSYLATION AT THR-71 AND ASN-91, DISULFIDE BONDS.
[16]	"Post-translational modification of bovine pro-opiomelanocortin. Tyrosine sulfation and pyroglutamate formation, a mass spectrometric study." Bateman A., Solomon S., Bennett H.P.J. J. Biol. Chem. 265:22130-22136(1990) [PubMed: 2266117] [Abstract] Cited for: SULFATION AT TYR-200, PYROGLUTAMATE FORMATION AT GLU-173.

Cross-references

Sequence databases
EMBLGenBankDDBJ	V00107 mRNA. Translation: CAA23441.1. V00107 mRNA. Translation: CAA23440.1. M25587 mRNA. Translation: AAA30354.1. J00021, J00019 Genomic DNA. Translation: AAB59262.1. BC122728 mRNA. Translation: AAI22729.1. M23814 mRNA. Translation: AAA30414.1. Different initiation. M10723 mRNA. Translation: AAA30718.1.
IPI	IPI00685204.
PIR	CTBOP. A93206.
RefSeq	NP_776576.1.
UniGene	Bt.8797
3D structure databases
ModBase	Search...
PTM databases
GlycoSuiteDB	P01190.
Genome annotation databases
Ensembl	ENSBTAG00000007897. Bos taurus. [Contig view]
GeneID	281416.
KEGG	bta:281416.
Phylogenomic databases
HOVERGEN	P01190.
OMA	P01190. GKKRRPV.
Family and domain databases
InterPro	IPR001941. Mcortin_ACTH. IPR013533. Mcortin_ACTH_C. IPR013531. Mcrtin_ACTH_cent. IPR013593. Melanocortin_N. IPR013532. Opioid_neuropept. [Graphical view]
PANTHER	PTHR11416. Mcortin_ACTH. 1 hit.
Pfam	PF00976. ACTH_domain. 1 hit. PF08384. NPP. 1 hit. PF08035. Op_neuropeptide. 1 hit. [Graphical view]
PRINTS	PR00383. MELANOCORTIN.
ProDom	PD003250. Mcortin_ACTH. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

COLI_BOVIN

Accession

Primary (citable) accession number: P01190
Secondary accession number(s): Q05B64 , Q28166, Q28167, Q28168

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)